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Disease relevance of Picornaviridae


High impact information on Picornaviridae

  • Since translation of FGF-2 mRNA was previously shown to occur by internal ribosome entry, a nonclassical mechanism already described for picornaviruses, the cross-linking patterns of FGF-2 and picornavirus mRNAs were compared [6].
  • A 49-amino-acid region of eIF-4 gamma, located in the N-terminal side of the site of cleavage by Picornaviridae protease 2A, was found to be sufficient for interacting with eIF-4E [7].
  • Compared to the control group, the immunoglobulin complementarity determining regions possess a relative excess of serine residues whereas picornaviruses suppress serine but overuse threonine residues, suggesting that the differing selective pressure has led to perturbations in the population of amino acid types on the surface of these proteins [8].
  • The functional properties of the nonstructural 2A protein are variable among different picornaviruses [2].
  • Poty- and picornaviruses share similar genome organizations and polyprotein processing strategies [9].

Chemical compound and disease context of Picornaviridae

  • Expression of polioviral protease 2A is sufficient to induce p220 cleavage, and the presence in 2A of an 18-amino-acid sequence representing a putative cysteine protease active site correlates with the ability of different picornaviruses to induce p220 cleavage [10].
  • These results suggest that there are differences in the involvement of COPI in the formation of the RCs of various picornaviruses, corresponding to their differential sensitivity to BFA [11].
  • The effect of bafilomycin A1 on other members of the Picornaviridae family was also assayed [12].
  • Site-directed mutagenesis experiments revealed that the RHDV protease closely resembles the 3C proteases of picornaviruses with respect to the amino acids directly involved in the catalytic activity as well as to the role played by histidine as part of the substrate binding pocket [13].
  • A tyrosine at this relative position is conserved among all calicivirus VPg proteins examined thus far, suggesting that the VPg protein of caliciviruses, like those of picornaviruses and potyviruses, utilizes tyrosine in the formation of a covalent bond with RNA [14].

Biological context of Picornaviridae


Gene context of Picornaviridae

  • These results suggest that the cleavage of PABP may be another mechanism by which picornaviruses alter the rate and spectrum of protein synthesis [20].
  • Three other regions in the PYFV polyprotein have sequence similarity to regions thought to have RNA polymerase, NTP-binding and protease functions in the polyproteins of picornaviruses, comoviruses and nepoviruses [21].
  • Infection of cells by picornaviruses results in proteolytic cleavage of eIF4G and generation of a cap-independent translational state [22].
  • Several picornaviruses shut down host cellular protein synthesis by proteolytic cleavage of the eukaryotic initiation factor (eIF) 4GI and eIF4GII isoforms [23].
  • Here we demonstrate that cytoplasmic expression of the serine protease inhibitor (serpin), plasminogen activator inhibitor type 2 (PAI-2), affords a high level of protection from lytic infection by multiple human picornaviruses [24].

Analytical, diagnostic and therapeutic context of Picornaviridae


  1. The structure of echovirus type 12 bound to a two-domain fragment of its cellular attachment protein decay-accelerating factor (CD 55). Bhella, D., Goodfellow, I.G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D.J., Lea, S.M. J. Biol. Chem. (2004) [Pubmed]
  2. Specific interaction between human parechovirus nonstructural 2A protein and viral RNA. Samuilova, O., Krogerus, C., Pöyry, T., Hyypiä, T. J. Biol. Chem. (2004) [Pubmed]
  3. Biochemical and genetic studies of the initiation of human rhinovirus 2 RNA replication: purification and enzymatic analysis of the RNA-dependent RNA polymerase 3D(pol). Gerber, K., Wimmer, E., Paul, A.V. J. Virol. (2001) [Pubmed]
  4. Guanidine-selected mutants of poliovirus: mapping of point mutations to polypeptide 2C. Pincus, S.E., Diamond, D.C., Emini, E.A., Wimmer, E. J. Virol. (1986) [Pubmed]
  5. Polypyrimidine tract-binding protein inhibits translation of bip mRNA. Kim, Y.K., Hahm, B., Jang, S.K. J. Mol. Biol. (2000) [Pubmed]
  6. Translation of CUG- but not AUG-initiated forms of human fibroblast growth factor 2 is activated in transformed and stressed cells. Vagner, S., Touriol, C., Galy, B., Audigier, S., Gensac, M.C., Amalric, F., Bayard, F., Prats, H., Prats, A.C. J. Cell Biol. (1996) [Pubmed]
  7. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. Mader, S., Lee, H., Pause, A., Sonenberg, N. Mol. Cell. Biol. (1995) [Pubmed]
  8. Analysis of antigenic surfaces of proteins. Lea, S., Stuart, D. FASEB J. (1995) [Pubmed]
  9. Uridylylation of the potyvirus VPg by viral replicase NIb correlates with the nucleotide binding capacity of VPg. Puustinen, P., Mäkinen, K. J. Biol. Chem. (2004) [Pubmed]
  10. Leader protein of foot-and-mouth disease virus is required for cleavage of the p220 component of the cap-binding protein complex. Devaney, M.A., Vakharia, V.N., Lloyd, R.E., Ehrenfeld, E., Grubman, M.J. J. Virol. (1988) [Pubmed]
  11. Differential requirements for COPI coats in formation of replication complexes among three genera of Picornaviridae. Gazina, E.V., Mackenzie, J.M., Gorrell, R.J., Anderson, D.A. J. Virol. (2002) [Pubmed]
  12. Entry of poliovirus into cells does not require a low-pH step. Pérez, L., Carrasco, L. J. Virol. (1993) [Pubmed]
  13. Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus. Boniotti, B., Wirblich, C., Sibilia, M., Meyers, G., Thiel, H.J., Rossi, C. J. Virol. (1994) [Pubmed]
  14. Mutagenesis of tyrosine 24 in the VPg protein is lethal for feline calicivirus. Mitra, T., Sosnovtsev, S.V., Green, K.Y. J. Virol. (2004) [Pubmed]
  15. Human rhinovirus-14 protease 3C (3Cpro) binds specifically to the 5'-noncoding region of the viral RNA. Evidence that 3Cpro has different domains for the RNA binding and proteolytic activities. Leong, L.E., Walker, P.A., Porter, A.G. J. Biol. Chem. (1993) [Pubmed]
  16. Cell proteins bind to a linear polypyrimidine-rich sequence within the 5'-untranslated region of rhinovirus 14 RNA. Rojas-Eisenring, I.A., Cajero-Juarez, M., del Angel, R.M. J. Virol. (1995) [Pubmed]
  17. The nucleotide sequence of sacbrood virus of the honey bee: an insect picorna-like virus. Ghosh, R.C., Ball, B.V., Willcocks, M.M., Carter, M.J. J. Gen. Virol. (1999) [Pubmed]
  18. Influence of polyions on the early steps of enterovirus infection. Mastromarino, P., Seganti, L., Petruzziello, R., Gabrieli, R., Divizia, M., Panà, A., Orsi, N. Journal of chemotherapy (Florence, Italy) (1991) [Pubmed]
  19. Chemical shift mapping of RNA interactions with the polypyrimidine tract binding protein. Yuan, X., Davydova, N., Conte, M.R., Curry, S., Matthews, S. Nucleic Acids Res. (2002) [Pubmed]
  20. Cleavage of Poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff? Kerekatte, V., Keiper, B.D., Badorff, C., Cai, A., Knowlton, K.U., Rhoads, R.E. J. Virol. (1999) [Pubmed]
  21. Sequence analysis of the parsnip yellow fleck virus polyprotein: evidence of affinities with picornaviruses. Turnbull-Ross, A.D., Mayo, M.A., Reavy, B., Murant, A.F. J. Gen. Virol. (1993) [Pubmed]
  22. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation. Lamphear, B.J., Kirchweger, R., Skern, T., Rhoads, R.E. J. Biol. Chem. (1995) [Pubmed]
  23. Human rhinovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different. Gradi, A., Svitkin, Y.V., Sommergruber, W., Imataka, H., Morino, S., Skern, T., Sonenberg, N. J. Virol. (2003) [Pubmed]
  24. Picornavirus receptor down-regulation by plasminogen activator inhibitor type 2. Shafren, D.R., Gardner, J., Mann, V.H., Antalis, T.M., Suhrbier, A. J. Virol. (1999) [Pubmed]
  25. Clinical activity of pleconaril in an experimentally induced coxsackievirus A21 respiratory infection. Schiff, G.M., Sherwood, J.R. J. Infect. Dis. (2000) [Pubmed]
  26. Heat-shock protein induction in adriamycin and picornavirus-infected cardiocytes. Huber, S.A. Lab. Invest. (1992) [Pubmed]
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